|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
1.32e-80 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 254.11 E-value: 1.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958683053 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
2.38e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 102.38 E-value: 2.38e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683053 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.27e-17 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 79.92 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1958683053 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-778 |
8.42e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSlrKELVA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELA--------NKYNGAVNEI 314
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeaelKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 315 KDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAD----NDFTNERLTALQERllSKSGGDCT 390
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenlEGFSEGVKALLKNQ--SGLSGILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 391 FIHQFIECQKK------LMVQGHLTKVVEESKLS-KENQAKAKESDLS-------DTLSPSKEKSSDDTTDAQMDEQ--- 453
Cdd:TIGR02168 524 VLSELISVDEGyeaaieAALGGRLQAVVVENLNAaKKAIAFLKQNELGrvtflplDSIKGTEIQGNDREILKNIEGFlgv 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 454 --DLNEPLAKVSLLKDDLQG--------------------------------------TQAETEAKQDTQHLRKELVEAQ 493
Cdd:TIGR02168 604 akDLVKFDPKLRKALSYLLGgvlvvddldnalelakklrpgyrivtldgdlvrpggviTGGSAKTNSSILERRREIEELE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 494 ELARASKQKCFDLQALL---EEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDT---EISSTRDKLLSAQDEI 567
Cdd:TIGR02168 684 EKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEI 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 568 LLLHQAAAKA---VSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTF---QLRCQQCE----------VQQ 631
Cdd:TIGR02168 764 EELEERLEEAeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLErriaaterrlEDL 843
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 632 REEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ 711
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 712 HlrdeADLKTLLSKAENQAKDVQkeyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 778
Cdd:TIGR02168 924 L----AQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
3.93e-15 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 72.72 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683053 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
2.24e-13 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 66.53 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1958683053 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
6.20e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 64.13 E-value: 6.20e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683053 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-770 |
8.69e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 239 ELVALQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNErtqeelrELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE-------EAKKAAEAAKAEAEA 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 317 LSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQadndfTNERLTALQERLLSKSGGDctfihqfi 396
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE-----DKKKADELKKAAAAKKKAD-------- 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 397 ECQKK---LMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQG 471
Cdd:PTZ00121 1422 EAKKKaeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 472 TQAETEAKQDTQHLRK--------ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDME 543
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKaeeakkadEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 544 NLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTdfmslQEELKKVRAELEGWRKAASEYEEEIRSLQstfQLR 623
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELK 1653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 624 CQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmtRKELEN 703
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL------KKAEEE 1727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 704 QMGSLKEQHLRDEADLKtllsKAENQAKDvQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 770
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKK----KAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.06e-12 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 62.89 E-value: 1.06e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1958683053 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-778 |
4.87e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELVALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 334 KGQAEKKELQ---AKIDDMEEKEQELQAKI-------EALQADNDFTNERLTALQERLLSKSGGDCtfIHQFIECQKKLM 403
Cdd:TIGR02168 373 RLEELEEQLEtlrSKVAQLELQIASLNNEIerlearlERLEDRRERLQQEIEELLKKLEEAELKEL--QAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 404 VQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKDDLQGTQA------- 474
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSGLSGILGvlselis 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 475 ------------------------ETEAKQDTQHLRK-----------------ELVEAQELARASKQKCFDLQALLEEE 513
Cdd:TIGR02168 531 vdegyeaaieaalggrlqavvvenLNAAKKAIAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKF 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 514 RKAYRNQVE------------ESAKQIQVLQVQLQRL-----------------HMDMENLQEEKDTEISSTRDKLLSAQ 564
Cdd:TIGR02168 611 DPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 565 DEILLLHQAAAKAVSERDTdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQRE----------- 633
Cdd:TIGR02168 691 EKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieel 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 634 ----------------EATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMT 697
Cdd:TIGR02168 767 eerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 698 RKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 777
Cdd:TIGR02168 847 IEELSEDIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
.
gi 1958683053 778 K 778
Cdd:TIGR02168 923 K 923
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.35e-11 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 61.53 E-value: 2.35e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958683053 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-748 |
2.66e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 241 VALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 321 LKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSggdctfihqfiecqk 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA--------------- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 401 klmvQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQ 480
Cdd:COG1196 432 ----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 481 DTQHLRKELVEAQELARA-----SKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISS 555
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAvavliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 556 TRDKLLS-AQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlrcqqcevqqREE 634
Cdd:COG1196 588 LAAALARgAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV---------------TLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 635 ATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLR 714
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
570 580 590
....*....|....*....|....*....|....
gi 1958683053 715 DEADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 748
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
7.30e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 59.20 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1958683053 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
452-778 |
3.65e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 452 EQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCfdlqalLEEERKAYRNQVEEsakqiqvl 531
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLAS-------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 532 qvqlqrlhmdMENLQEEKDTEISSTRDKLLSAQDeilLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEE 611
Cdd:TIGR02169 249 ----------LEEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 612 EIRSLQStfqlRCQQCEVQ---QREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL------HNSQK 682
Cdd:TIGR02169 316 ELEDAEE----RLAKLEAEidkLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrdeLKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 683 QSLE-LTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSK---AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK 758
Cdd:TIGR02169 392 EKLEkLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340
....*....|....*....|
gi 1958683053 759 QSITDELKQCKDNLKLLREK 778
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRE 491
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-720 |
5.49e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNtedec 286
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS----- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 287 thlrEMNERTQEELRELANKyNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAK---IDDMEEKEQELQAKIEAL 363
Cdd:pfam15921 441 ----ECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEAT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 364 QADNDFTNERLT-ALQERLLSKSGGDcTFIHQFIECQKKLMVQGHLTKVVEESKLSKEN--QAKAKESDLSDTLSPSKEK 440
Cdd:pfam15921 516 NAEITKLRSRVDlKLQELQHLKNEGD-HLRNVQTECEALKLQMAEKDKVIEILRQQIENmtQLVGQHGRTAGAMQVEKAQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 441 SSDDTTDAQMDEQDLNeplakvsLLKDDLQGTQAETEAKQDTQHLRK-ELVEA-QELARASKQkcfdlqalLEEERKAYR 518
Cdd:pfam15921 595 LEKEINDRRLELQEFK-------ILKDKKDAKIRELEARVSDLELEKvKLVNAgSERLRAVKD--------IKQERDQLL 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 519 NQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEillLHQAAAKAVSERDTDFMSLQEELkkvrae 598
Cdd:pfam15921 660 NEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE---LEQTRNTLKSMEGSDGHAMKVAM------ 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 599 leGWRKAASEYEEEIRSLQSTFQLrCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELH 678
Cdd:pfam15921 731 --GMQKQITAKRGQIDALQSKIQF-LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVA 807
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1958683053 679 NSQ----KQSLELTSDLSILQmtRKELENQmgSLKEQHLRDEADLK 720
Cdd:pfam15921 808 NMEvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-622 |
1.06e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 211 DRLLSRLEVMGNQLQACSKNQTEdsLRKELVALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 291 EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEgkqeeiqqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 371 NERLTALQERLLSksggdctfihqfiECQKKLMVQGHLTKVVEESKLSKENQAKAKESdlSDTLSPSKEKSSDDTTDAQM 450
Cdd:TIGR02168 816 NEEAANLRERLES-------------LERRIAATERRLEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 451 DEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTqhLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAkqiqv 530
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSE--LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL----- 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 531 lqvqlqrlhMDMENLQEEKDTEISSTRDKLLSAQDEIL------LLHQAAAKAVSERdTDFMSLQ-EELKKVRAELEgwr 603
Cdd:TIGR02168 954 ---------EEAEALENKIEDDEEEARRRLKRLENKIKelgpvnLAAIEEYEELKER-YDFLTAQkEDLTEAKETLE--- 1020
|
410 420
....*....|....*....|
gi 1958683053 604 KAASEYEEEIRS-LQSTFQL 622
Cdd:TIGR02168 1021 EAIEEIDREARErFKDTFDQ 1040
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-759 |
2.76e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 204 WQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTE 283
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEE--LEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 284 DECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEAL 363
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 364 QAdndFTNERLTALQERLLSKSGgdctfIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSD 443
Cdd:COG1196 382 EE---LAEELLEALRAAAELAAQ-----LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 444 DTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEE 523
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 524 SAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQdEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEgWR 603
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA-TFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-EA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 604 KAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQ 683
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 684 SLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKT-QTVLSELKLKFEMTEQEKQ 759
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeEEALEELPEPPDLEELERE 768
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-770 |
3.99e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 235 SLRKELVALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLREMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQ---AKIDDMEEKEQELQAKIEAL--QADNDFTNErltalqerllsksgg 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLnnQKEQDWNKE--------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 388 dctfIHQFIECQKKlmvqghlTKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKD 467
Cdd:TIGR04523 312 ----LKSELKNQEK-------KLEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 468 DLQGTQAETEA-KQDTQHLRKELVEAQELARASKQKCFDLQA---LLEEERKAYRNQVEESAKQIQvlqvqlqrlhmDME 543
Cdd:TIGR04523 378 ENQSYKQEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK-----------DLT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 544 NLQEEKDTEISSTRDKLLSAQDEILLLhqaaAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlr 623
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL------- 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 624 cqqceVQQREEATRLQGELEKLKKEwdvLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKEL 701
Cdd:TIGR04523 516 -----TKKISSLKEKIEKLESEKKE---KESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683053 702 ENQMGSLKEQ--HLRDEADLKT-LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 770
Cdd:TIGR04523 588 QELIDQKEKEkkDLIKEIEEKEkKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-752 |
6.15e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.80 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQE---ELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 333 QKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLM-VQGHLTKV 411
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISeFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 412 VEESK-LSK-ENQAKAKESDLSDTL----------SPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DDLQGTQA- 474
Cdd:pfam01576 172 EEKAKsLSKlKNKHEAMISDLEERLkkeekgrqelEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEELQAALAr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 475 -ETEAKQDTQHLRK---------ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMEN 544
Cdd:pfam01576 252 lEEETAQKNNALKKireleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 545 LQ----EEK---DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQ 617
Cdd:pfam01576 332 LKkaleEETrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 618 ST---FQLRCQQCEVQQREEA---TRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDL 691
Cdd:pfam01576 412 GQlqeLQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683053 692 silqmtrKELENQMGSLKEQhlrdeadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 752
Cdd:pfam01576 492 -------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
9.77e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.58 E-value: 9.77e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958683053 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-650 |
1.19e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 263 QEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQ--EELRELANKYNGAVNEIKDLSDKLKAAEGKQEEiqqkgqAEKK 340
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELRELELALLVLRLEELR------EELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 341 ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLsksggdctfihqfiECQKKLMVQGHLTKVVEESKLSKE 420
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE--------------ELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 421 NQAKAKESDLSDTlspskekssddTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAkqdtqhLRKELVEAQELARASK 500
Cdd:TIGR02168 309 ERLANLERQLEEL-----------EAQLEELESKLDELAEELAELEEKLEELKEELES------LEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 501 QKCFDLQALLEEERKAY---RNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISS-TRDKLLSAQDEILLLHQAAAK 576
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEE 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683053 577 AVSERDTdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQStfqlRCQQCEVQQREEATRLQGELEKLKKEWD 650
Cdd:TIGR02168 452 LQEELER----LEEALEELREELEEAEQALDAAERELAQLQA----RLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-600 |
1.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQED 246
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 247 KHSYETTAKESLRRVLQEKievvRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG1196 423 LEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 327 KQEEIQQKGQAEKKELQAK--------IDDMEEKEQELQAKIEA-----LQADNDFTNERLTALQERLLSKSGGDCTFIH 393
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAglrglagaVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 394 QFIECQKKLMVQGHLTKVVEESKL---SKENQAKAKESDLSDTLSpskekssDDTTDAQMDEQDLNEPLAKVSLLKDDLQ 470
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDlvaSDLREADARYYVLGDTLL-------GRTLVAARLEAALRRAVTLAGRLREVTL 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 471 GTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKD 550
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958683053 551 TEisstRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELE 600
Cdd:COG1196 732 AE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-683 |
1.47e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 336 QAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSggdctfihqfiecqkklmVQGHLTKVVEES 415
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS------------------RQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 416 KLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAkqdtqhLRKELVEAQEL 495
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------LREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 496 ARASKQKCFDLQalleEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEkdteisstRDKLLSAQDEILLLHQAAA 575
Cdd:TIGR02168 812 LTLLNEEAANLR----ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--------IEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 576 KAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQ---STFQLRCQQCEVqqreeatRLQGELEKLKKEWDVL 652
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklAQLELRLEGLEV-------RIDNLQERLSEEYSLT 952
|
330 340 350
....*....|....*....|....*....|.
gi 1958683053 653 ENECRSLKKENVLLSSELQRQEKELHNSQKQ 683
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
1.71e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 53.00 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1958683053 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-773 |
2.13e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELVALQEDKHSYETTAKESLRRV--LQEKIE-V 268
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEkL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 269 VRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKE---LQAK 345
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 346 IDDMEEKEQELQAKIEALQADNDFTNERLT---ALQERLLSKSGGDCTFIHQFIECQKKLMVQ------GHLTKVVEES- 415
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASIQGVHGTVAQLGSVGERYATAievaagNRLNNVVVEDd 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 416 -------KLSKE-----------NQAKAKESDLS------------------------------DTLSpskeKSSDDTTD 447
Cdd:TIGR02169 558 avakeaiELLKRrkagratflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgDTLV----VEDIEAAR 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 448 AQMD-------EQDLNEP---------------------LAKVSLLKDDLQGTQAETEA-KQDTQHLRKELVEAQELARA 498
Cdd:TIGR02169 634 RLMGkyrmvtlEGELFEKsgamtggsraprggilfsrsePAELQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSD 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 499 SKQKCFDLQA---LLEEERKAYRNQVEESAKQIQVlqvqlqrLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLHQ 572
Cdd:TIGR02169 714 ASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSS-------LEQEIENVKSELKEleaRIEELEEDLHKLEEALNDLEA 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 573 aaakavSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQ---------------LRCQQCEVQQREEATR 637
Cdd:TIGR02169 787 ------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiqelqeqridLKEQIKSIEKEIENLN 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 638 -----LQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQH 712
Cdd:TIGR02169 861 gkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 713 LRDEADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkDNLK 773
Cdd:TIGR02169 941 GEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
546-778 |
4.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 546 QEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQL--- 622
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 623 ---RCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK 699
Cdd:COG1196 296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 700 ELENQMGSLKEQHL---RDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 776
Cdd:COG1196 376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
..
gi 1958683053 777 EK 778
Cdd:COG1196 456 EE 457
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.88e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 49.87 E-value: 4.88e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683053 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
5.91e-08 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 52.03 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1958683053 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
485-767 |
1.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 485 LRKELVEAQELARASKQKcfdlqaLLEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmENLQEEKDTEISSTRDKLLSAQ 564
Cdd:COG1196 218 LKEELKELEAELLLLKLR------ELEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 565 DEILLLHQAAAKAVSERD---TDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevqqrEEATRLQGE 641
Cdd:COG1196 288 AEEYELLAELARLEQDIArleERRRELEERLEELEEELAELEEELEELEEELEELE---------------EELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 642 LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKT 721
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958683053 722 LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 767
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
258-760 |
1.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 258 LRRVLQ-EKIE-VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKG 335
Cdd:PRK03918 151 VRQILGlDDYEnAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 336 QaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERL--LSKSGGDCTFIHQFIECQKKLmvqghltKVVE 413
Cdd:PRK03918 231 K-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKL-------SEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 414 ESKLSKENQAKAKESDLSDTLSPSKEKSSddttDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVE-A 492
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 493 QELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQ 572
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 573 AAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEY------EEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLK 646
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELiklkelAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 647 KEWDVLENECRS---LKKENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMTRKELE---NQMGSLK--EQHLRDE- 716
Cdd:PRK03918 539 GEIKSLKKELEKleeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKdaEKELEREe 618
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1958683053 717 ---ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 760
Cdd:PRK03918 619 kelKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-777 |
2.48e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLRE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 292 MNERTQEELRELANKyngavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 372 eRLTALQERLLSKSggdctfihqfiecqkklmvqghltkvvEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMD 451
Cdd:TIGR00606 465 -QLEGSSDRILELD---------------------------QELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 452 EQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVL 531
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKL 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 532 QVQLQRLhmdmENLQEEKDTEISSTRDKLLSAQDEILllhqaAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEE 611
Cdd:TIGR00606 597 NKELASL----EQNKNHINNELESKEEQLSSYEDKLF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 612 EIRSLQSTFQLRCQQC------EVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLL-------SSELQRQEKELH 678
Cdd:TIGR00606 668 FITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIP 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 679 NSQKQSLELTSDLSILQMTRKELENQMGSL--KEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMT 754
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQV 827
|
570 580
....*....|....*....|...
gi 1958683053 755 EQEKQSITDELKQCKDNLKLLRE 777
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRK 850
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-773 |
6.37e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 228 SKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELR-ELA 304
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKaEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 305 NKYNGA--VNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQaKIEALQADNDftnERLTALQERll 382
Cdd:PTZ00121 1176 KKAEAArkAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAE---EAKKAEEER-- 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 383 sksggDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQaKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKv 462
Cdd:PTZ00121 1250 -----NNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK- 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 463 sllkddlqgtQAEtEAKQDTQHLRKELVEAQ---ELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLH 539
Cdd:PTZ00121 1323 ----------KAE-EAKKKADAAKKKAEEAKkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 540 MDMEnlQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQST 619
Cdd:PTZ00121 1392 KADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 620 FQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQK----QSLELTSDLSILQ 695
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkaDEAKKAEEKKKAD 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 696 MTRKELENQMGSLK---EQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVL-SELKLKFEMT--EQEKQSITDELKQCK 769
Cdd:PTZ00121 1550 ELKKAEELKKAEEKkkaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYeEEKKMKAEEAkkAEEAKIKAEELKKAE 1629
|
....
gi 1958683053 770 DNLK 773
Cdd:PTZ00121 1630 EEKK 1633
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
7.89e-07 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 48.00 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1958683053 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-778 |
8.61e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 298 EELRELANKYNGAVNEIkdLSDKLKAAEGKQEEIQQKgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 378 QERLlsksggdctfiHQFIECQKKLMVqghLTKVVEESKLSKENQAKAKEsDLSDTLSPSKEKSSD--DTTDAQMDEQDL 455
Cdd:PRK02224 240 DEVL-----------EEHEERREELET---LEAEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 456 NEPLAK-VSLLKDDLQGTQAET-----EAKQDTQHLRKELVEAQELARAskqkcfdlqalLEEERKAYRNQVEEsakqiq 529
Cdd:PRK02224 305 DDADAEaVEARREELEDRDEELrdrleECRVAAQAHNEEAESLREDADD-----------LEERAEELREEAAE------ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 530 vlqvqlqrlhmdMENLQEEKDTEISSTRDKLLSAQDEIlllhQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEY 609
Cdd:PRK02224 368 ------------LESELEEAREAVEDRREEIEELEEEI----EELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 610 EEEIRSLQSTF----QLR----CQQCE------------VQQREEATRLQGELEKLKKEWDVLENECRSLKkenvllssE 669
Cdd:PRK02224 432 EATLRTARERVeeaeALLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------D 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 670 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 749
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
490 500 510
....*....|....*....|....*....|....*
gi 1958683053 750 KFEMTEQEKQS------ITDELKQCKDNLKLLREK 778
Cdd:PRK02224 580 KLAELKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-702 |
9.07e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 228 SKNQTEDSLRKELVALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQE--- 298
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElke 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 299 ------ELRELANKYNGAVNEIKDLSDKLKA-AEGKQEEIQQkgqAEKKElqAKIDDMEEKEQELQAKIEALQADNDfTN 371
Cdd:PRK03918 291 kaeeyiKLSEFYEEYLDELREIEKRLSRLEEeINGIEERIKE---LEEKE--ERLEELKKKLKELEKRLEELEERHE-LY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 372 ERLTALQERL--LSKSGGDCTfihqfIECQKKLM--VQGHLTKVVEESK--LSKENQAKAKESDLSDTLSPSKE-KSSDD 444
Cdd:PRK03918 365 EEAKAKKEELerLKKRLTGLT-----PEKLEKELeeLEKAKEEIEEEISkiTARIGELKKEIKELKKAIEELKKaKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 445 TTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQdtQHLRKELVEAQ-ELARASK----QKCFDLQALLEEERKAYR- 518
Cdd:PRK03918 440 VCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKE--RKLRKELRELEkVLKKESEliklKELAEQLKELEEKLKKYNl 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 519 NQVEESAKQIQVLQVQLQRLHMDMENLQEE--KDTEISSTRDKLLSAQDEIL-----LLHQAAAKAVSERDTDFMSLQEe 591
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKEleKLEELKKKLAELEKKLDELEeelaeLLKELEELGFESVEELEERLKE- 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 592 LKKVRAELEGWRKAASEYEEEIRSLQStfqlrCQQCEVQQREEATRLQGELEKLKKEWDVL-----ENECRSLKKENVLL 666
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKK-----LEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLEL 671
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958683053 667 SSELQRQEKELHNSQKQSLELTSDLSILQMTRKELE 702
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-773 |
1.30e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 347 DDMEEKEQE---LQAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLmvqgHLTKVVEESKLSKENQA 423
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL----NLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 424 KAKESDLSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgtqaetEAKQDTQHLRKELVEAQELARASKQKC 503
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 504 FDLQALLEEERKayrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKD--------TEISSTRDKLLSAQDEILLLHQAAA 575
Cdd:TIGR04523 263 NKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkSELKNQEKKLEEIQNQISQNNKIIS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 576 ----------KAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKL 645
Cdd:TIGR04523 339 qlneqisqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 646 KKEWDVLENECRSLKKENVLLSSE------------------------------------------LQRQEKELHNSQKQ 683
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEikdltnqdsvkeliiknldntresletqlkvlsrsinkikqnLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 684 SLELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMteQEKQSITD 763
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIE 571
|
570
....*....|
gi 1958683053 764 ELKQCKDNLK 773
Cdd:TIGR04523 572 ELKQTQKSLK 581
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-739 |
1.45e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 229 KNQTEDSLRK---ELVALQEDKHSY--ETTAKESLRRVLQEKIEVVRKLSEVERSLSNtedecthLREMNERTQEELREL 303
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHInnELESKEEQLSSYEDKLFDVCGSQDEESDLER-------LKEEIEKSSKQRAML 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 304 ANKYNGAVNEIKDLSDKLKAAEgkqeEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNdftnERLTALQERLLS 383
Cdd:TIGR00606 659 AGATAVYSQFITQLTDENQSCC----PVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESEL----KKKEKRRDEMLG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 384 KSGGDCTFIHQFIECQKKLmvQGHLTKVVEEskLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQ---DLNEPLA 460
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPEL--RNKLQKVNRD--IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfqmELKDVER 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 461 KVSLLKDDLQGTqaetEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHM 540
Cdd:TIGR00606 807 KIAQQAAKLQGS----DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 541 --DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQS 618
Cdd:TIGR00606 883 rqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 619 TFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKenvllSSELQRQEKELHNSQKQSLELTSDLSILQMTR 698
Cdd:TIGR00606 963 KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEEL 1037
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958683053 699 KELENQMG-----SLKEQHLRDEADLKtLLSKAENQAKDVQKEYEK 739
Cdd:TIGR00606 1038 KQHLKEMGqmqvlQMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-662 |
1.67e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 335 GQA---EKKELQAKIDDMEEKEQELQAKIEALQADNDftnerltalqerllsksggdctfiHQFIEcqkklMVQGHLTKV 411
Cdd:TIGR02169 753 IENvksELKELEARIEELEEDLHKLEEALNDLEARLS------------------------HSRIP-----EIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 412 VEESKlskenqakakesdlsdtlspSKEKSSDDTtdaqmdEQDLNEPLAKVSLLKDDLQGTQAETEakqDTQHLRKELVE 491
Cdd:TIGR02169 804 EEEVS--------------------RIEARLREI------EQKLNRLTLEKEYLEKEIQELQEQRI---DLKEQIKSIEK 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 492 AQELARASKQKcfdlqalLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLH 571
Cdd:TIGR02169 855 EIENLNGKKEE-------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKL 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 572 QAAAKAVSERDTDFMSLQEE------LKKVRAELEgwrkaasEYEEEIRSLQSTFQLRCQQCEvqqrEEATR---LQGEL 642
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQ-------RVEEEIRALEPVNMLAIQEYE----EVLKRldeLKEKR 995
|
410 420
....*....|....*....|...
gi 1958683053 643 EKLKKEWDVLE---NECRSLKKE 662
Cdd:TIGR02169 996 AKLEEERKAILeriEEYEKKKRE 1018
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.83e-06 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 47.35 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1958683053 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.92e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 46.64 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1958683053 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
2.08e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 46.97 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1958683053 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-777 |
3.46e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 237 RKELVA--LQEDKHSYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLREMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 306 KYNGAVNEIKDLSDKLKAAegkqeeiqqkgqaeKKELQAKIDDMEEKEQElqaKIEALQADNDFtneRLTALQERLLSKS 385
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEAL--------------KSESQNKIELLLQQHQD---RIEQLISEHEV---EITGLTEKASSAR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 386 ggdctfihqfiecQKKLMVQGHLTKVVEESKlskeNQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLL 465
Cdd:pfam15921 292 -------------SQANSIQSQLEIIQEQAR----NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 466 KDDLqgTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRlHMDMENL 545
Cdd:pfam15921 355 NSEL--TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDR-NMEVQRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 546 QEEKDTEISSTRDKLLSAQDEILLLHQAAAKaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQ 625
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEK-VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 626 QCEVQQrEEATRLQG-------ELEKLKKEWDVLEN---ECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQ 695
Cdd:pfam15921 511 AIEATN-AEITKLRSrvdlklqELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 696 MTRKELENQMG----SLKE-QHLRDEADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 770
Cdd:pfam15921 590 VEKAQLEKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN 667
|
....*..
gi 1958683053 771 NLKLLRE 777
Cdd:pfam15921 668 ELNSLSE 674
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.76e-06 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 46.16 E-value: 3.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683053 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
455-778 |
3.87e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 455 LNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKElveAQELARaskqkcfdlqallEEERkayRNQVEESAKQIQVLQVQ 534
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---KEEKAR-------------EVER---RRKLEEAEKARQAEMDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 535 LQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELK--KVRAELEGWRKAASEYEEE 612
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKneRVRQELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 613 IRSLQStfQLRCQQCEVQQREEATrlQGELEKLKKEwdvLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDls 692
Cdd:pfam17380 412 QRKIQQ--QKVEMEQIRAEQEEAR--QREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 693 ilQMTRKELENQMGSLKEQHLRDEadlKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ-EKQSITDELKQCKDN 771
Cdd:pfam17380 483 --KRDRKRAEEQRRKILEKELEER---KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQ 557
|
....*..
gi 1958683053 772 LKLLREK 778
Cdd:pfam17380 558 MRKATEE 564
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
585-778 |
5.29e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 585 FMSLQEELKKVRAELegWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATrLQGELEKLKKEWDVLENECRSLKKENV 664
Cdd:COG1196 215 YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 665 LLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVL 744
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190
....*....|....*....|....*....|....
gi 1958683053 745 SELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 778
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
231-775 |
5.64e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 231 QTEDSLRKELVALQEDKHSYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEEL-RELANKYNG 309
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 310 AVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKEL------QAKIDDMEEKEQELQAKIEALQAD-------NDFTNERLTA 376
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSElrqarkrRDQASEALRQ 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 377 LQERLLSKSGGDCTFIHQFIE-----------------------CQKKLMVQGHLTKVVEESKLSKEN----------QA 423
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPqagtllhflrkeapdweqsigkvISPELLHRTDLDPEVWDGSVGGELnlygvkldlkRI 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 424 KAKES-DLSDTLSPSKEKSSDDTTDAQMDEQDLNEPL--AKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASK 500
Cdd:pfam12128 591 DVPEWaASEEELRERLDKAEEALQSAREKQAAAEEQLvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 501 QKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKA--- 577
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAelk 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 578 --VSERDTDFMS----------LQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQRE---EATRLQGEL 642
Cdd:pfam12128 751 alETWYKRDLASlgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNierAISELQQQL 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 643 EKLKKEwdvlenecrslkkenvllsSELQRQ--EKELHNSQKQSLELTSDLSILqmtrKELENQMGSLKEQHLRDEAD-- 718
Cdd:pfam12128 831 ARLIAD-------------------TKLRRAklEMERKASEKQQVRLSENLRGL----RCEMSKLATLKEDANSEQAQgs 887
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683053 719 -------LKTLLSKAENQAKDVQKEYEKTQTVL-----SELKLKFEMTEQEKQSITDELKQCKDNLKLL 775
Cdd:pfam12128 888 igerlaqLEDLKLKRDYLSESVKKYVEHFKNVIadhsgSGLAETWESLREEDHYQNDKGIRLLDYRKLV 956
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
588-778 |
6.88e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 588 LQEELKKVRAELEGWRKAASEYeeeiRSLQSTFQLRCQQCEVQQREEatrLQGELEKLKKEWDVLENECRSLKKENVLLS 667
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY----RELKEELKELEAELLLLKLRE---LEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 668 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLlskaENQAKDVQKEYEKTQTVLSEL 747
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 1958683053 748 KLKFEMTEQEKQSITDELKQCKDNLKLLREK 778
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-365 |
8.55e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKhsyetTAK 255
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----ERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 256 ESLRRVLQEKIEVVR---------KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958683053 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-580 |
8.84e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 310 AVNEIKDLSDKLKAAEGKQEEIQqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKsggdc 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 390 tfihqfiecqkklmvqghltkvveESKLSKENQAKAKESDLSDTLspskekssddttDAQMDEQDLNEPLAKVSLLKddl 469
Cdd:COG3883 85 ------------------------REELGERARALYRSGGSVSYL------------DVLLGSESFSDFLDRLSALS--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 470 QGTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEK 549
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250 260 270
....*....|....*....|....*....|.
gi 1958683053 550 DTEISSTRDKLLSAQDEILLLHQAAAKAVSE 580
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-381 |
1.84e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 233 EDSLRKELVALQEDKhsyettakESLRRVLQEKIEVVRKLSEVER--SLSNTEDECTHLR--EMNERTQEELRELANKYN 308
Cdd:COG4942 85 LAELEKEIAELRAEL--------EAQKEELAELLRALYRLGRQPPlaLLLSPEDFLDAVRrlQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683053 309 GAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERL 381
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.15e-05 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 44.18 E-value: 2.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.46e-05 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 44.08 E-value: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683053 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.82e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.48 E-value: 2.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683053 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.14e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.43 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1958683053 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.16e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1958683053 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-763 |
3.81e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 253 TAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDEctHLREMNERtQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEI 331
Cdd:pfam05483 197 LAFEELRvQAENARLEMHFKLKEDHEKIQHLEEE--YKKEINDK-EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 332 QQKGQAEKKELQAKIddmeEKEQELQAKIEALQADNDFTNERLTALQERLLSKSggdcTFIHQFIECQKKLMVQGHLTKV 411
Cdd:pfam05483 274 EEKTKLQDENLKELI----EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT----KTICQLTEEKEAQMEELNKAKA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 412 VEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKD----DLQGTQAETEAKQDTQHLRK 487
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnkevELEELKKILAEDEKLLDEKK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 488 ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENlQEEKDTEISSTRDKLLSAQDEI 567
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKLLLENKEL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 568 LLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQ--CEVQQREEATR-LQGELEK 644
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkCKLDKSEENARsIEYEVLK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 645 LKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLS 724
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958683053 725 KAENQAKDVQKEYEKTQTVLSE-LKLKFEMTEQEKQSITD 763
Cdd:pfam05483 665 DKKISEEKLLEEVEKAKAIADEaVKLQKEIDKRCQHKIAE 704
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-778 |
4.01e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 567 ILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQRE-EATRLQGELEKL 645
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--RIAALARRIRALEqELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 646 KKEWDVLENECRSLKKE-----------------NVLLSSE-LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 707
Cdd:COG4942 89 EKEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683053 708 LKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 778
Cdd:COG4942 169 LEAER----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
541-780 |
5.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 541 DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStf 620
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEK-LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 621 QLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK- 699
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 700 --ELENQMGSLKEQHLRDEaDLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 777
Cdd:PRK03918 347 lkELEKRLEELEERHELYE-EAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1958683053 778 KGN 780
Cdd:PRK03918 420 EIK 422
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
419-781 |
6.30e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 419 KENQAKakesDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKElveaqELARA 498
Cdd:pfam05483 252 KENKMK----DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE-----DLQIA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 499 SKQKCfdlqaLLEEERKAyrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEisstRDKLLSAQDEILLLHQAAAKAV 578
Cdd:pfam05483 323 TKTIC-----QLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRLEKNEDQLKIITMELQKKS 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 579 SERD--TDFMSLQE----ELKKVRAELEGWRKAASEYEEEIRSLQSTFQlrcqqcevqqreeatRLQGELEKLKKEWDVL 652
Cdd:pfam05483 391 SELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ---------------ELIFLLQAREKEIHDL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 653 ENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSL--------------KEQHLRDEAD 718
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQEERMLKQ 535
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683053 719 LKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 781
Cdd:pfam05483 536 IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.80e-05 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 42.22 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1958683053 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
7.21e-05 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 42.70 E-value: 7.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683053 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
555-751 |
8.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 555 STRDKLLSAQDEILLLHQAAAKAVSERDTdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQcevQQREE 634
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 635 ATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLR 714
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958683053 715 DEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKF 751
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
573-767 |
1.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 573 AAAKAVSERDTDFMSLQEELKKVRAE---LEGWRKAASEYEE------EIRSLQSTFQL--------RCQQCEVQQREEA 635
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQielLEPIRELAERYAAarerlaELEYLRAALRLwfaqrrleLLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 636 TRLQGELEKLKKEWDVLENECRSLKKE------NVL--LSSELQRQEKELHNsqkqsleltsdlsiLQMTRKELENQMGS 707
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQirgnggDRLeqLEREIERLERELEE--------------RERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 708 LKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 767
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.39e-04 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 41.54 E-value: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683053 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-777 |
1.65e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 567 ILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRcqqcevQQREEATRLQGELEKLK 646
Cdd:COG4942 8 ALLLALAAAAQADAAA----EAEAELEQLQQEIAELEKELAALKKEEKALLK--QLA------ALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 647 KEWDVLENECRSLKKENVLLSSELQRQEKELHN------------------SQKQSLELTSDLSILQMTRKELENQMGSL 708
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683053 709 KEQhLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMT----EQEKQSITDELKQCKDNLKLLRE 777
Cdd:COG4942 156 RAD-LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEA 227
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
1.80e-04 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 41.51 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
574-790 |
1.97e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 574 AAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQ-REEATRLQGELEKLKKEwdvL 652
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA--ELEALQAEIDKlQAEIAEAEAEIEERREE---L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 653 ENECRSLKKE-------NVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmtRKELENQMGSLKEQhlrdEAD 718
Cdd:COG3883 89 GERARALYRSggsvsylDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683053 719 LKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNNPSILQPVPA 790
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-711 |
2.23e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 472 TQAETEAKQDTQHLRKELVEAQELARASKQKcfdlQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEekdt 551
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 552 EISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevQQ 631
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 632 REEATRLQGELEKLKKEWDVLENEcrsLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ 711
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-501 |
2.70e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELVALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 282 TEDECTH----LREMNER----TQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ---QKGQAEKKELQAKIDDME 350
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 351 EKEQELQAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKL--------MVQGHLTKVVEESKLSKENQ 422
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreinELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 423 A--KAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQH-LRKELVEAQELARAS 499
Cdd:TIGR02169 423 AdlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSkLQRELAEAEAQARAS 502
|
..
gi 1958683053 500 KQ 501
Cdd:TIGR02169 503 EE 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
238-380 |
3.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 238 KELVALQEDKHSYETTAKESLRRV--LQEKIE-VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEI 314
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIerLEERREdLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683053 315 KDLSDKLKAAEGKQEEIQQKGQAEKK--ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQER 380
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER 635
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-381 |
3.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 234 DSLRKELVALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERL 381
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-523 |
3.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 236 LRKELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthlremnerTQEELRELANKYNgavnE 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS-----------AEREIAELEAELE----R 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 314 IKDLSDKLKAAEGKQEEIQqkgqAEKKELQAKIDDMEEKEQELQAKIEALQadndftnERLTALQERLLSKSGGDCTFIH 393
Cdd:COG4913 680 LDASSDDLAALEEQLEELE----AELEELEEELDELKGEIGRLEKELEQAE-------EELDELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 394 QFIECQ-KKLMVQGHLTKVVE--ESKLSKENQAKAK-ESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDl 469
Cdd:COG4913 749 ALLEERfAAALGDAVERELREnlEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED- 827
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683053 470 qgtqaeteakqdtqhlrkELVEAQE-----LARASKQKCFDLQALLEEERKAYRNQVEE 523
Cdd:COG4913 828 ------------------GLPEYEErfkelLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-756 |
4.77e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 162 SQELFQLSQYLQEAL--HRE--QMLEQKLATLQRL---LAITQEASDTSWQALIDE-DRLLSRLEVMGNQL--------- 224
Cdd:pfam10174 69 NQHLQLTIQALQDELraQRDlnQLLQQDFTTSPVDgedKFSTPELTEENFRRLQSEhERQAKELFLLRKTLeemelriet 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 225 QACSKNQTEDSLRKELVALQEDKHSYETTAKESLRRvlQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELA 304
Cdd:pfam10174 149 QKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERT--RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 305 N-KYNGAVNEIKDlsDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQA----------KIEALQADNDFTNER 373
Cdd:pfam10174 227 KtKALQTVIEMKD--TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQELSKKESE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 374 LTALQERL--LSKSGGDCtfiHQFIECQKK-LMVQGHLTKVVEESKLSKENQAKAKESDL---SDTLSPSKEKSSDDTTD 447
Cdd:pfam10174 305 LLALQTKLetLTNQNSDC---KQHIEVLKEsLTAKEQRAAILQTEVDALRLRLEEKESFLnkkTKQLQDLTEEKSTLAGE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 448 AQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKqDTQ--HLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESA 525
Cdd:pfam10174 382 IRDLKDMLDVKERKINVLQKKIENLQEQLRDK-DKQlaGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 526 KQIQVLQVQLQRLHMDMENLQEEKDteiSSTRDKLLSAQDEILLLHQAAAKAVS--ERDTDFMSLQEELKKVRAE---LE 600
Cdd:pfam10174 461 REDRERLEELESLKKENKDLKEKVS---ALQPELTEKESSLIDLKEHASSLASSglKKDSKLKSLEIAVEQKKEEcskLE 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 601 GWRKAASEYEEEIR-SLQSTFQLRCQQCEVQQ-REEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELH 678
Cdd:pfam10174 538 NQLKKAHNAEEAVRtNPEINDRIRLLEQEVARyKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQN 617
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683053 679 NSQKQsleltsdlsiLQMTRKELENQMGSLKEQHLRDEADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 756
Cdd:pfam10174 618 KKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
4.83e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 39.93 E-value: 4.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683053 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
5.01e-04 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 40.49 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1958683053 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
591-777 |
5.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 591 ELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKL---KKEWDVLENECRSLKKENVLLS 667
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 668 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELEN---------QMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYE 738
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958683053 739 KtqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 777
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
5.31e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELVALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 284 decTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKK---ELQAKIDDMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1958683053 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
467-677 |
5.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 467 DDLQGTQAETE-AKQDTQHLRkELVEAQELARASKQKCFDLQALLEEeRKAYRNQVEesakqiqvlqvqLQRLHMDMENL 545
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRR------------LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 546 QEEK---DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQST--- 619
Cdd:COG4913 301 RAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPlpa 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683053 620 --------------FQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL 677
Cdd:COG4913 378 saeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
5.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELV 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 242 ALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4913 696 ELEAEL----EELEEELDELKGEIGRLEKELEQAEEELDELQDR---LEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*..
gi 1958683053 322 KAAEGKQEEIQQKGQAEKKELQAKIDD 348
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-362 |
5.97e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 235 SLrkELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLREMNERTQEELRELANkyngAV 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958683053 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEA 362
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.27e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.59 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1958683053 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-600 |
6.93e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 273 SEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAkiddMEEK 352
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 353 EQELQAKIEALQADNDFTNERLTALQERlLSKSGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSD 432
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEER-LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 433 TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQH--LRKELVEAQELARASKQKCFDLQAL- 509
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEseLEALLNERASLEEALALLRSELEELs 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 510 -----LEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEkdteisstrdklLSAQDEILLlhQAAAKAVSERDTD 584
Cdd:TIGR02168 901 eelreLESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER------------LSEEYSLTL--EEAEALENKIEDD 966
|
330
....*....|....*.
gi 1958683053 585 FMSLQEELKKVRAELE 600
Cdd:TIGR02168 967 EEEARRRLKRLENKIK 982
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
590-764 |
7.07e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 590 EELKKVRAELEGWRKAASEYEEEIRSLQSTFQlRCQQCEvQQREEATRLQGELEKLKKEWDVLEnECRSLKKENVLLSSE 669
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELE-AELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 670 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 749
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 1958683053 750 KFEMTEQEKQSITDE 764
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
165-767 |
7.44e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 165 LFQLSQYLQEALHREQMLEQKLATLQRLLaiTQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKN---------QTEDS 235
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELR--AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQaqrihtelqSKMRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 236 LRKELVALQE-DKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEI 314
Cdd:TIGR00618 323 RAKLLMKRAAhVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 315 KDLSD---KLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERllSKSGGDCTF 391
Cdd:TIGR00618 403 DILQReqaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER--EQQLQTKEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 392 IHQFIECQKKLMVQGHLTKVVEESKLSK---ENQAKAKESDLSDTLSP---------SKEKSSDDTTDAQMDE--QDLNE 457
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGsciHPNPARQDIDNPGPLTRrmqrgeqtyAQLETSEEDVYHQLTSerKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 458 PLAKVSLLKDDLQG-TQAETEAKQDTQHLRKELVEAQ----ELARASKQKCFDLQALLEEERKAYRNQ--VEESAKQIQV 530
Cdd:TIGR00618 561 LKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQdlteKLSEAEDMLACEQHALLRKLQPEQDLQdvRLHLQQCSQE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 531 LQVQLQRLHMDMENLQEEKDTEISstrdkLLSAQDEILLLHQAAAKAVSERdtdfmSLQEELKKVRAELEGWRKAASEYE 610
Cdd:TIGR00618 641 LALKLTALHALQLTLTQERVREHA-----LSIRVLPKELLASRQLALQKMQ-----SEKEQLTYWKEMLAQCQTLLRELE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 611 EEIRSLQSTFQLRCQQCEVQQREeatrLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSD 690
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSD----LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 691 LSILQMTRKELENQMGSLKEQHlrdEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 767
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.50e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 39.40 E-value: 7.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683053 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-538 |
7.61e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 297 QEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQkgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTA 376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 377 LQERLlsksggdctfihqfiECQKKLMvqghltkvveeSKLSKENQAKAKESDLSDTLSPskEKSSDDTTDAQMDEQDLN 456
Cdd:COG4942 95 LRAEL---------------EAQKEEL-----------AELLRALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 457 EPLAKVSLLKDDLQG----TQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQ 532
Cdd:COG4942 147 ARREQAEELRADLAElaalRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
....*.
gi 1958683053 533 VQLQRL 538
Cdd:COG4942 227 ALIARL 232
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
634-757 |
7.97e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.00 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 634 EATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmtrkELENQMGSLKeqhl 713
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958683053 714 rdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 757
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-387 |
8.52e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 234 DSLRKELVALQEDKHSYET--TAKESLRRVLQEKIEVVR-KLSEV--ERSLSNTEDECTHLREMNERTQEELRELANKYN 308
Cdd:COG1579 41 AALEARLEAAKTELEDLEKeiKRLELEIEEVEARIKKYEeQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIE 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683053 309 GAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEalqadndftnERLTALQERLLSKSGG 387
Cdd:COG1579 121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP----------PELLALYERIRKRKNG 189
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
339-760 |
8.63e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 339 KKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSGGDctfiHQFIECQKKLMVQGHLTKVVEESKLS 418
Cdd:pfam05557 15 QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKRE----AEAEEALREQAELNRLKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 419 KENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETeakQDTQHLRKELVEAQELARA 498
Cdd:pfam05557 91 KLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA---SEAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 499 SKQKCFDLQalleeerkaYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISstrdKLLSAQDEILLLHQAAA--K 576
Cdd:pfam05557 168 AEQRIKELE---------FEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK----HLNENIENKLLLKEEVEdlK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 577 AVSERDTDFM----SLQEELKKVRAELEGWRKAASEYEEEIRS--LQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWD 650
Cdd:pfam05557 235 RKLEREEKYReeaaTLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 651 VLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMTRKELENQMGSlkEQHLRDEADLKTLLSKA 726
Cdd:pfam05557 315 ELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEEAEDMTQKM 392
|
410 420 430
....*....|....*....|....*....|....
gi 1958683053 727 ENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 760
Cdd:pfam05557 393 QAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
480-648 |
9.57e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 480 QDTQHLRKELVEAQELARASKQKCFDLQALLeeERKAYRNqVEESAKQIQVLQVQLQRLHMDMENLQEEKDTeissTRDK 559
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQRDAKQQAFALTEVV--QRRAHFS-YEDAAEMLAKNSDLNEKLRQRLEQAEQERTR----AREQ 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 560 LLSAQDEILLLHQAAAKAVSERDTDFMSLQE---ELKK--VRAElEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQ---Q 631
Cdd:PRK04863 1008 LRQAQAQLAQYNQVLASLKSSYDAKRQMLQElkqELQDlgVPAD-SGAEERARARRDELHARLSANRSRRNQLEKQltfC 1086
|
170
....*....|....*..
gi 1958683053 632 REEATRLQGELEKLKKE 648
Cdd:PRK04863 1087 EAEMDNLTKKLRKLERD 1103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-761 |
9.60e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQ---ADNDFTNERLT--------ALQERLLSKSGGDCTFIHQF 395
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 396 IECQKKLMVQG-HLTKVVEESKLSKENQAK------------AKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKV 462
Cdd:TIGR00618 316 LQSKMRSRAKLlMKRAAHVKQQSSIEEQRRllqtlhsqeihiRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 463 SLLKDDLQGTQAEtEAKQDTQHLRkELVEAQELARASKQkCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDM 542
Cdd:TIGR00618 396 QSLCKELDILQRE-QATIDTRTSA-FRDLQGQLAHAKKQ-QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 543 ENLQE-----EKDTEISSTRDKLLSAQDE--------ILLLHQAAAKA-VSERDTDFM--------SLQEELKKVRAELE 600
Cdd:TIGR00618 473 QQLQTkeqihLQETRKKAVVLARLLELQEepcplcgsCIHPNPARQDIdNPGPLTRRMqrgeqtyaQLETSEEDVYHQLT 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 601 GWRKAASEYEEEIRSLQSTFQlRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQ----RQEKE 676
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 677 LHNSQKQSLEltsDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 756
Cdd:TIGR00618 632 LHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
....*
gi 1958683053 757 EKQSI 761
Cdd:TIGR00618 709 LETHI 713
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
590-781 |
9.82e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 590 EELKKVRAELEGWRKAASEYEEEIRSLQstfQLRCQQcevQQREEATRLQGELEKLKKEWDVLENEcrslkKENVLLSSE 669
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE---PIRELA---ERYAAARERLAELEYLRAALRLWFAQ-----RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 670 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQmgsLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 749
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190
....*....|....*....|....*....|..
gi 1958683053 750 KFEMTEQEKQSITDELKQCKDNLKLLREKGNN 781
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-705 |
1.01e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELVALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 262 LQEKIEVVRKLSE------VERSLSNTEDECTHLR-----EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEerddllAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 331 IQQKGQAEKKELQA---KIDDMEEKEQELQAKIEALQADNDFTNERLTALQERL------LSKSGGDCTFIHQFIECQKK 401
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLeelreeRDELREREAELEATLRTARE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 402 LMVQGHltKVVEESKLSKENQaKAKESDLSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEA 478
Cdd:PRK02224 441 RVEEAE--ALLEAGKCPECGQ-PVEGSPHVETIEEDRERVEEleaELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 479 KQDTQHL---RKELVEAQELARASKQK-CFDLQALLEEERKAYRNQVEESAKQIQVLQVQlqrlhmdmenlqEEKDTEIS 554
Cdd:PRK02224 518 REDLEELiaeRRETIEEKRERAEELRErAAELEAEAEEKREAAAEAEEEAEEAREEVAEL------------NSKLAELK 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 555 STRDKLLSAQDEILLLHQAAAKAVSERdtdfmslqeELKKVRAELEGWRKAA-SEYEEEIRSLQSTFQLRCQQCEVQQRE 633
Cdd:PRK02224 586 ERIESLERIRTLLAAIADAEDEIERLR---------EKREALAELNDERRERlAEKRERKRELEAEFDEARIEEAREDKE 656
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683053 634 EAT----RLQGELEKLKKEWDVLENECRSLkkENVLLSSELQRQEKELHNSQKQSLE-LTSDLSILQMTRKELENQM 705
Cdd:PRK02224 657 RAEeyleQVEEKLDELREERDDLQAEIGAV--ENELEELEELRERREALENRVEALEaLYDEAEELESMYGDLRAEL 731
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
608-778 |
1.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 608 EYEEEIRSLQSTFQLRCQQCEVQQR--EEATRLQGE-LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsqkqs 684
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKniEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED----- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 685 leLTSDLSILQMTRKELENQMGSL-KEQHLRDEADL-----------KTLLSKAENQAKDVQKEYEKTQTVLSELKLKF- 751
Cdd:PHA02562 253 --PSAALNKLNTAAAKIKSKIEQFqKVIKMYEKGGVcptctqqisegPDRITKIKDKLKELQHSLEKLDTAIDELEEIMd 330
|
170 180
....*....|....*....|....*....
gi 1958683053 752 EMTEQEK--QSITDELKQCKDNLKLLREK 778
Cdd:PHA02562 331 EFNEQSKklLELKNKISTNKQSLITLVDK 359
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-382 |
1.19e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 274 EVERSLSNTEDECTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958683053 341 ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLL 382
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELR 409
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
1.24e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKdlsdklKAAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAK------KEADEIIKELRQL 596
|
90 100 110
....*....|....*....|....*....|.
gi 1958683053 335 GQAEKKELQAKidDMEEKEQELQAKIEALQA 365
Cdd:PRK00409 597 QKGGYASVKAH--ELIEARKRLNKANEKKEK 625
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-551 |
1.32e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 328 QEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLlsksggdctfihQFIECQKKLMVQGH 407
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI------------RALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 408 LTKVVEESKLskENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQhlrK 487
Cdd:COG4942 86 AELEKEIAEL--RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL---A 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683053 488 ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDT 551
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.39e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 38.60 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.58e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 39.34 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683053 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-385 |
1.60e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 180 QMLEQKLATLQRLLAITQEASDTSWQALideDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKHSYETTAKESLR 259
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAEL---EELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 260 rVLQEKIEVVRKLSEVERSLSNTE--DECTHLREMNERTQEELRELANkyngAVNEIKDLSDKLKAAEGKQEEIQQKGQA 337
Cdd:COG3883 94 -ALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958683053 338 EKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKS 385
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
630-778 |
1.64e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 630 QQREEATR----LQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELEN 703
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKllLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 704 QMGS----------------LKEQHLRDEADLKTLLSK----------AENQAKDVQKEYEK-TQTVLSELKLKFEMTEQ 756
Cdd:COG3206 248 QLGSgpdalpellqspviqqLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQeAQRILASLEAELEALQA 327
|
170 180
....*....|....*....|..
gi 1958683053 757 EKQSITDELKQCKDNLKLLREK 778
Cdd:COG3206 328 REASLQAQLAQLEARLAELPEL 349
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
632-758 |
1.95e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 632 REEATRLQGELEKLKKEWDVLENECRSLKK----ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 707
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958683053 708 LKEQhlrdEADLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 758
Cdd:smart00787 244 LTNK----KSELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
510-683 |
2.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 510 LEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmenlqEEKDTEISSTRDKLLSAQDEILLLHQAAA-KAVSERDTDFMSL 588
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 589 QEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSS 668
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 1958683053 669 ELQRQEKELHNSQKQ 683
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
2.75e-03 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 40.90 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1958683053 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
3.18e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 237 ---RKELVALQEDKHSYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958683053 314 IKDLSDKLkaaegkqeeiqqkgQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG0497 322 LLAYAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
232-775 |
3.41e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 232 TEDSLRKELVALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR-EMNERTQ---------EE 299
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKvieilrqqiEN 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 300 LRELANKYNGAVNEIKDLSDKL-KAAEGKQEEIQQ------KGQAEKKELQAKIDDME-EKEQELQAKIEALQADNDFTN 371
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLeKEINDRRLELQEfkilkdKKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQ 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 372 ERLTALQERLLSKSggDCTFIHQFIECQKKLMVQGHLTKVVEESKLskENQAKAKESDLSDTLSPSKEKSSDDTTDAQMD 451
Cdd:pfam15921 654 ERDQLLNEVKTSRN--ELNSLSEDYEVLKRNFRNKSEEMETTTNKL--KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 452 ---EQDLNEPLAKVSLLKDDLQG-TQAETEAKQDTQHLRKELVE-AQELARASKQK---CFDLQALLEEERKAYRN---- 519
Cdd:pfam15921 730 mgmQKQITAKRGQIDALQSKIQFlEEAMTNANKEKHFLKEEKNKlSQELSTVATEKnkmAGELEVLRSQERRLKEKvanm 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 520 ---------QVEESAKQIQVLQVQLQRLHM----DMENLQEEKDTEISSTRDKLL-------------SAQDEILLL--H 571
Cdd:pfam15921 810 evaldkaslQFAECQDIIQRQEQESVRLKLqhtlDVKELQGPGYTSNSSMKPRLLqpasftrthsnvpSSQSTASFLshH 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 572 QAAAKAVSERDT-DFMSLQEELKKV----------RAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQG 640
Cdd:pfam15921 890 SRKTNALKEDPTrDLKQLLQELRSVineeptvqlsKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSK 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 641 ELEKLKKE-----WDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSlELTSDLSILQMTRKELENQMGSLKEQHLRD 715
Cdd:pfam15921 970 SSETCSREpvllhAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKS-PVHSLLTSSAEGSIGSSSQYRSAKTIHSPD 1048
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683053 716 EA-DLKTL-LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLL 775
Cdd:pfam15921 1049 SVkDSQSLpIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQEKML 1110
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
258-365 |
3.77e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 258 LRRVLQEKIEVV---RKLSEVERSLSntEDECTHLREMNERTQ----EELRELANKYNGAVNEIKDLSDKLKAAEGKQ-- 328
Cdd:PRK05771 1 LAPVRMKKVLIVtlkSYKDEVLEALH--ELGVVHIEDLKEELSnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKkk 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958683053 329 ------EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:PRK05771 79 vsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ 121
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
337-683 |
5.23e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.43 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 337 AEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSksggdctfihqfiECQKKlMVQGHLTKVV---- 412
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLD-------------ECWKK-IKRKKNSALSealn 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 413 ----EESKLSKENQAKAKESDLSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQGTQAETEAK 479
Cdd:pfam13166 155 gfkyEANFKSRLLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVIGKSSAIEEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 480 QDTQHLRKELVEAQELARASKQKC-F---DLQALLEEERKAYRNQ-VEEsakqiqvlqvqlqrlhmDMENLQEEKDTEIS 554
Cdd:pfam13166 235 IKNPDLADWVEQGLELHKAHLDTCpFcgqPLPAERKAALEAHFDDeFTE-----------------FQNRLQKLIEKVES 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 555 STRDKL--LSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRK---AASEYE------EEIRSLQST---- 619
Cdd:pfam13166 298 AISSLLaqLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDsvdakiESINDLVASinel 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683053 620 ----------FQLRCQQCEVQ-QREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQ 683
Cdd:pfam13166 378 iakhneitdnFEEEKNKAKKKlRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQ 452
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-494 |
6.89e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 289 LREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAD-- 366
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEll 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 367 -------------NDFTNER-LTALQERLLSK------SGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAK 426
Cdd:PHA02562 245 nlvmdiedpsaalNKLNTAAaKIKSKIEQFQKvikmyeKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683053 427 EsdlsdtlspskEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGTQAetEAKQdtqhLRKELVEAQE 494
Cdd:PHA02562 325 L-----------EEIMDEFNEQSKKLLELK---NKISTNKQSLITLVD--KAKK----VKAAIEELQA 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-622 |
7.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 212 RLLSRLEVMGNQLQACSKNQTEdsLRKELVALQEDKHSYETTAK-ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR 290
Cdd:COG4717 92 ELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 291 EMNERTQEELRELANKYNGAV-NEIKDLSDKLKAAegkqeeiqqkgQAEKKELQAKIDDMEEKEQELQAKIEALQAD--N 367
Cdd:COG4717 170 AELAELQEELEELLEQLSLATeEELQDLAEELEEL-----------QQRLAELEEELEEAQEELEELEEELEQLENEleA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 368 DFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLMVQGHLTKVV-----EESKLSKENQAKAKESDLSDTLsPSKEKSS 442
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllalLFLLLAREKASLGKEAEELQAL-PALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 443 DDTTDAQMDEQDLNEPLAK---VSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLE--EERKAY 517
Cdd:COG4717 318 EEELEELLAALGLPPDLSPeelLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 518 RNQVEESAKQIQVLQVQLQRLHMDMENLQEEK-DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTdfMSLQEELKKVR 596
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELL 475
|
410 420
....*....|....*....|....*.
gi 1958683053 597 AELEGWRKAASEYEEEIRSLQSTFQL 622
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLALEL 501
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
325-710 |
9.09e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 39.35 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 325 EGKQEEIQQKGQA--EKKELQAKIDDMEEKEQELQAKIEalQADNdftnERLTALQERLLSKSGgdctfihqfiecqkkl 402
Cdd:pfam09731 85 EKKQVKIPRQSGVssEVAEEEKEATKDAAEAKAQLPKSE--QEKE----KALEEVLKEAISKAE---------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 403 mvqgHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqGTQAETEAKQDt 482
Cdd:pfam09731 143 ----SATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINL-----AKQSEEEAAPP- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 483 qhlrkELVEAQELARASkqkcfdLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLS 562
Cdd:pfam09731 213 -----LLDAAPETPPKL------PEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 563 AQDEILL-------LHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcEVQQREEa 635
Cdd:pfam09731 282 NDDLNSLiahahreIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAAD----------EAQLRLE- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683053 636 trLQGELEKLKKEWD-VLENECRSLKKENVL-LSSELQRQEKELHNSQKQSLE---------LTSDLSILQMTRKELENQ 704
Cdd:pfam09731 351 --FEREREEIRESYEeKLRTELERQAEAHEEhLKDVLVEQEIELQREFLQDIKekveeeragRLLKLNELLANLKGLEKA 428
|
....*.
gi 1958683053 705 MGSLKE 710
Cdd:pfam09731 429 TSSHSE 434
|
|
| |
